Current Protein Identity:P49799
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1AGR COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4 Deposited 1997-03-25 | Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain E
1–205(205 aa)
|
Not recorded | MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 CIT CITRIC ACID × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.3;THE COMPLEX WAS CRYSTALLIZED IN HANGING DROPS USING PEG 10000 AS THE PRECIPITANT AND SODIUM CITRATE PH 5.3 AS THE BUFFER., vapor diffusion - hanging drop
|
Resolution 2.80 Å R-free 0.291 |
| 1AGR COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4 Deposited 1997-03-25 | Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain H
1–205(205 aa)
|
Not recorded | MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 CIT CITRIC ACID × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.3;THE COMPLEX WAS CRYSTALLIZED IN HANGING DROPS USING PEG 10000 AS THE PRECIPITANT AND SODIUM CITRATE PH 5.3 AS THE BUFFER., vapor diffusion - hanging drop
|
Resolution 2.80 Å R-free 0.291 |
| 1EZT HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR Deposited 2000-05-11 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
51–205(155 aa)
Fragment:CORE RGS DOMAIN
|
Not recorded | No recorded non-water small molecule | SOLUTION NMR |
NMR measurement conditions
pH 6;303 K;Ionic strength (raw mmCIF value) 50 mM K;Pressure ambient
NMR sample composition
1 mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0 | 90% H2O/10% D2O
NMR sample composition
1 mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0 | 100% D2O
NMR sample composition
1 mM RGS4 U-15N; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0 | 90% H2O/10% D2O
|
Resolution not provided |
| 1EZY HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR Deposited 2000-05-12 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
51–205(155 aa)
Fragment:CORE DOMAIN OF RGS
|
Not recorded | No recorded non-water small molecule | SOLUTION NMR |
NMR sample composition
1mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0 | 90% H2O/10% D2O
NMR sample composition
1mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0 | 100% D2O
NMR sample composition
1mM RGS4 U-15N; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0 | 90% H2O/10% D2O
|
Resolution not provided |